ID A0A091DCI5_FUKDA Unreviewed; 262 AA.
AC A0A091DCI5;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Tomoregulin-2 {ECO:0000313|EMBL:KFO27985.1};
GN ORFNames=H920_10666 {ECO:0000313|EMBL:KFO27985.1};
OS Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Fukomys.
OX NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO27985.1, ECO:0000313|Proteomes:UP000028990};
RN [1] {ECO:0000313|EMBL:KFO27985.1, ECO:0000313|Proteomes:UP000028990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Liver {ECO:0000313|EMBL:KFO27985.1};
RA Gladyshev V.N., Fang X.;
RT "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT African mole rats.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the tomoregulin family.
CC {ECO:0000256|ARBA:ARBA00038484}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR EMBL; KN122834; KFO27985.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091DCI5; -.
DR STRING; 885580.ENSFDAP00000000719; -.
DR eggNOG; KOG3649; Eukaryota.
DR Proteomes; UP000028990; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR CDD; cd00104; KAZAL_FS; 1.
DR Gene3D; 3.30.60.30; -; 1.
DR Gene3D; 2.10.25.10; Laminin; 1.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR002350; Kazal_dom.
DR InterPro; IPR036058; Kazal_dom_sf.
DR PANTHER; PTHR21632:SF5; TRANSMEMBRANE PROTEIN WITH EGF LIKE AND TWO FOLLISTATIN LIKE DOMAINS 2; 1.
DR PANTHER; PTHR21632; UNCHARACTERIZED; 1.
DR Pfam; PF07648; Kazal_2; 1.
DR SMART; SM00280; KAZAL; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR SUPFAM; SSF100895; Kazal-type serine protease inhibitors; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS51465; KAZAL_2; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000028990};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 207..229
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 69..117
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 149..189
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 241..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..262
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 179..188
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 262 AA; 29159 MW; 836FE7D1ADB7E2E3 CRC64;
MDRVIATASS EFTSPSGKIS KHLPTSNCPL TEMQFHEGSG ETSQKETSTC DICQFGAECD
EDAEDVWCVC NIDCSQTNFN PLCASDGKSY DNACQIKEAS CQKQEKIEVM SLGRCQDNTT
TTTKSEDGHY ARTDYAENAN KLEESAREHH IPCPEHYNGF CMHGKCEHSI NMQEPSCRCD
AGYTGQHCEK KDYSVLYVVP GPVRFQYVLI AAVIGTVQIA VICVVVLCIT RKCPRSNRIH
RQKQNTGHYS SDNTTRASTR LI
//
